summary:Protein splicing is a post-translational process that results in excision of an internal protein region (intein) and ligation of its flanking sequences (exteins). Protein splicing does not require cofactors of host's enzymes: it is catalyzed by itself through the internal domain (Hint-domain) [a]. It can be explained by tertiary structure of intein. The distance between the N and C ends of the intein is comparable with the length of a covalent bond (about 1.4 Å). Hint-domain plays an important role in autocatalytic cleavage of the intein and subsequent ligation of the exteins. Interestingly, that the Hint-domain catalytic center structurally is similar to the active center of serine protease.

The main aims of our work was to create intein-based chimeric protein for quick purification of the human growth hormone (HGH). I made a chimeric protein consisting of a short N-terminal peptide, the Mxe GyrA intein, and human growth hormone between them. I did quick affinity purification by the intein, and then induce self-cleavage of the intein, that releases human growth hormone in a pure buffer [b, c].

Second place for the presentation "Optimization of recombinant protein obtaining and purification using protein splicing" on Conference of Young Scientists "Actual problems of biochemistry and biotechnology - 2006", Kiev, Ukraine;

First place award in the category of "Best cycle of scientific publication in field of biotechnology" given by Institute of Molecular biology and Genetics of NAS of Ukraine